4e9v: Difference between revisions

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 ==Multicopper Oxidase mgLAC (data1)==
-<StructureSection load='4e9v' size='340' side='right' caption='[[4e9v]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
+<StructureSection load='4e9v' size='340' side='right'caption='[[4e9v]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
 == Structural highlights ==
 <table><tr><td colspan='2'>[[4e9v]] is a 3 chain structure with sequence from [http://en.wikipedia.org/wiki/Uncultivated_bacterium Uncultivated bacterium]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4E9V OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4E9V FirstGlance]. <br>
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 <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4e9v FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4e9v OCA], [http://pdbe.org/4e9v PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4e9v RCSB], [http://www.ebi.ac.uk/pdbsum/4e9v PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4e9v ProSAT]</span></td></tr>
 </table>
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+Structural models determined by X-ray crystallography play a central role in understanding the catalytic mechanism of enzymes. However, X-ray radiation generates hydrated electrons that can cause significant damage to the active sites of metalloenzymes. In the present study, crystal structures of the multicopper oxidases (MCOs) CueO from Escherichia coli and laccase from a metagenome were determined. Diffraction data were obtained from a single crystal under low to high X-ray dose conditions. At low levels of X-ray exposure, unambiguous electron density for an O atom was observed inside the trinuclear copper centre (TNC) in both MCOs. The gradual reduction of copper by hydrated electrons monitored by measurement of the Cu K-edge X-ray absorption spectra led to the disappearance of the electron density for the O atom. In addition, the size of the copper triangle was enlarged by a two-step shift in the location of the type III coppers owing to reduction. Further, binding of O2 to the TNC after its full reduction was observed in the case of the laccase. Based on these novel structural findings, the diverse resting structures of the MCOs and their four-electron O2-reduction process are discussed.
+New insights into the catalytic active-site structure of multicopper oxidases.,Komori H, Sugiyama R, Kataoka K, Miyazaki K, Higuchi Y, Sakurai T Acta Crystallogr D Biol Crystallogr. 2014 Mar;70(Pt 3):772-9. doi:, 10.1107/S1399004713033051. Epub 2014 Feb 22. PMID:24598746<ref>PMID:24598746</ref>
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
+</div>
+<div class="pdbe-citations 4e9v" style="background-color:#fffaf0;"></div>
+== References ==
+<references/>
 __TOC__
 </StructureSection>
+[[Category: Large Structures]]
 [[Category: Uncultivated bacterium]]
 [[Category: Higuchi, Y]]